SMART: Pfam domain DUF2228

The domain within your query sequence starts at position 77 and ends at position 328; the E-value for the DUF2228 domain shown below is 7e-117.

GLRLVGPYDILAGKHKMKKKPTGLNCNLHWRFYYDPPEFQTIIIGDNKTQYHMGYFRDSP
DELPVYVGTNEAKKNCIIIQNGDNVFAAIKLFLMKKLKEVTDRKKISILKNIDEKLTEAA
RKLGYSLEQRTVKMRQRDKKVVTKTFHGAGLVVPVDKNDVGYRELPETDADLKRICKAVV
DAASDEERLKAFAPIQEMMTFVQFANDECDYGMGLELGMDLFCYGSHYFHKVAGQLLPLA
YNLLKRDLFAKI

DUF2228

PFAM accession number:	PF10228
Interpro abstract (IPR019361):	Histone PARylation factor 1 (HPF1, previously known as C4orf27) is a key regulator of ADP-ribosylation signaling in response to DNA damage. It has been demonstrated that HPF1 forms a complex with PARP-1 (poly(ADP-ribose) polymerase 1) and is recruited to DNA lesions in a PARP-1-dependent manner, but independently of PARP-1 catalytic ADP-ribosylation activity. HPF1 has also been shown limit DNA damage-induced hyper-automodification of PARP-1 by promoting PARP-1-dependent in trans ADP-ribosylation of histones [ (PUBMED:27067600) ].

PFAM accession number:

PF10228

Interpro abstract (IPR019361):

Histone PARylation factor 1 (HPF1, previously known as C4orf27) is a key regulator of ADP-ribosylation signaling in response to DNA damage. It has been demonstrated that HPF1 forms a complex with PARP-1 (poly(ADP-ribose) polymerase 1) and is recruited to DNA lesions in a PARP-1-dependent manner, but independently of PARP-1 catalytic ADP-ribosylation activity. HPF1 has also been shown limit DNA damage-induced hyper-automodification of PARP-1 by promoting PARP-1-dependent in trans ADP-ribosylation of histones [ (PUBMED:27067600) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DUF2228